Each antibody in the Silent Synapses Antibody Sampler Kit detects its target protein at endogenous levels. The phospho-specific antibodies recognizehuman AMPA Receptor 1 (GluA1) only when phosphorylated at the indicated residues. While the literature refers to the GluA1 phospho-residues as Ser831 and Ser845, the corresponding residues for UniProt ID #P42261 are Ser849 and Ser863, respectively.

Western Blotting

Western Blotting

Western blot analysis of extracts from mouse brain and rat brain using Phospho-AMPA Receptor 1 (GluA1) (Ser845) (D10G5) Rabbit mAb. The phospho-specificity of the antibody was verified by blocking with a phospho or nonphosphopeptide.

IF-F

AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are composed of four subunits (GluA1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluA2-containing AMPARs, AMPARs that lack GluA2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties and surface expression of AMPARs representing key pathways to mediate synaptic plasticity (3). During development and mature states, some synapses exhibit “silent synapses” that lack functional AMPAR-mediated transmission. Synapses become “unsilenced” by post-translational modification of GluAs, particularly GluA1, which alters its kinetic properties and/or surface expression while other synaptic components, such as other glutamate receptors like NMDARs and postsynaptic scaffolding proteins like PSD95, remain unaltered. Conversely, reducing the AMPAR kinetic properties and surface expression can silence synapses. Key post-translational modifications implicated in regulating these processes include phosphorylation of GluA1 at Ser831 and Ser845 (4). Research studies have implicated activity-dependent changes in AMPARs in a variety of diseases, including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).